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Muscle and liver pyruvate kinases are closely related: amino acid sequence comparisons

1984; Wiley; Volume: 171; Issue: 2 Linguagem: Inglês

10.1016/0014-5793(84)80507-4

1873-3468

Colin G. Hoar, Gordon W. Nicoll, Emile Schiltz, Wilfried Schmitt, David P. Bloxham, Michael F. Byford, B. Dunbar, Linda A. Fothergill,

Protein Structure and Dynamics

Previous evidence has shown that the M 1 and L pyruvate kinase isozymes differ markedly in kinetic and immunological properties, amino acid compositions and peptide maps. However, the amino acid sequence results we present here for the N‐terminal region and for a region of the C domain show that the M 1 and L isozymes are very similar. The variable length of the N‐terminal sequences also explains the difference in regulation by phosphorylation between the M 1 and L isozymes. The M 1 isozyme lacks the serine residue that has been shown to be phosphorylated in the L isozyme.